Rapid degradation of a large fraction of newly synthesized proteins by proteasomes

Nature

Volumn 404, Issue 6779, 2000, Pages 770-774

  Schubert, Ulrich ^a,b   Antón, Luis C ^a   Gibbs, James ^a   Norbury, Christopher C ^a   Yewdell, Jonathan W ^a   Bennink, Jack R ^a  

^a NATIONAL INSTITUTE OF ALLERGY AND INFECTIOUS DISEASES   (United States)

^b UNIVERSITY OF HAMBURG   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

GAG PROTEIN; MAJOR HISTOCOMPATIBILITY ANTIGEN CLASS 1; PROTEASOME; VIRUS PROTEIN;

ARTICLE; ENDOPLASMIC RETICULUM; HUMAN; HUMAN CELL; PRIORITY JOURNAL; PROTEIN ASSEMBLY; PROTEIN DEGRADATION; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN PROCESSING; PROTEIN SYNTHESIS; PROTEIN TRANSPORT;

ANIMALS; CELL LINE; CYSTEINE ENDOPEPTIDASES; CYSTEINE PROTEINASE INHIBITORS; DENDRITIC CELLS; GENE PRODUCTS, GAG; HELA CELLS; HISTOCOMPATIBILITY ANTIGENS CLASS I; HUMANS; LEUPEPTINS; MICE; MULTIENZYME COMPLEXES; PEPTIDE BIOSYNTHESIS; PROTEASOME ENDOPEPTIDASE COMPLEX; PROTEIN BIOSYNTHESIS; PROTEIN PRECURSORS; PROTEINS; UBIQUITINS;

HUMAN IMMUNODEFICIENCY VIRUS;

EID: 0034643336     PISSN: 00280836     EISSN: None     Source Type: Journal    
DOI: 10.1038/35008096     Document Type: Article

References (18)

1. Rock, K. L. & Goldberg, A. L. Degradation of cell proteins and the generation of MHC class I-presented peptides. Annu. Rev. Immunol. 17, 739-779 (1999).
2. Pamer, E. & Cresswell, P. Mechanisms of MHC class I restricted antigen processing. Annu. Rev. Immunol. 16, 323-358 (1998).
3. Yewdell, J. W., Antón, L. C. & Bennink, J. R. Defective ribosomal products (DRiPs). A major source of antigenic peptides for MHC class I molecules? J. Immunol. 157, 1823-1826 (1996).
4. Fenteany, G. et al. Inhibition of proteasome activities and subunit-specific amino-terminal threonine modification by lactacystin. Science 268, 726-731 (1995).
5. Rock, K. L. et al. Inhibitors of the proteasome block the degradation of most cell proteins and the generation of peptides presented on MHC class I molecules. Cell 78, 761-771 (1994).
6. Vinitsky, A., Michaud, C., Powers, J. C. & Orlowski, M. Inhibition of the chymotrypsin-like activity of the pituitary multicatalytic proteinase complex. Biochemistry 31, 9421-9428 (1992).
7. Fujimuro, M., Sadada, H. & Yokosawa, H. Production and characterization of monoclonal antibodies specific to multi-ubiquitin chains of polyubiquitinated proteins. FEBS Lett. 349, 173-180 (1994).
8. Wojcik, C., Schroeter, D., Wilk, S., Lamprecht, J. & Paweletz, N. Ubiquitin-mediated proteolysis centers in HeLa cells: indication from studies of an inhibitor of the chymotrypsin-like activity of the proteasome. Eur. J. Cell Biol. 71, 311-318 (1996).
9. Johnston, J. A., Ward, C. L. & Kopito, R. R. Aggresomes: a cellular response to misfolded proteins. J. Cell. Biol. 143, 1883-1898 (1998).
10. Anton, L. C. et al. Intracellular localization of proteasomal degradation of a viral antigen. J. Cell Biol. 146, 113-124 (1999).
11. Steinman, R. M. in Fundamental Immunology (ed. Paul, W. E.) 547-604 (Lippincolt-Raven, Philadelphia, 1998).
12. Townsend, A. et al. Association of class I major histocompatibility heavy and light chains induced by viral peptides. Nature 340, 443-448 (1989).
13. Degen, E. & Williams, D. B. Participation of a novel 88-kD protein in the biogenesis of murine class I histocompatibility molecules. J. Cell Biol. 112, 1099-1115 (1991).
14. Reits, E. A. J., Vos, J. C., Grommé, M. & Neefjes, J. The major substrates for TAP in vivo are derived from newly synthesized proteins. Nature 404, 774-778 (2000).
15. Rammensee, H. -G., Bachmann, J. & Stevanovic, S. MHC Ligands and Peptide Motifs (Landes Bioscience, Austin, 1997).
16. Engelhard, V. H. Structures of peptides associated with class I and class II MHC molecules. Annu. Rev. Immunol. 12, 181-207 (1994).
17. Alberts, B. et al. Molecular Biology of the Cell (Garland, New York, 1994).
18. Adachi, A. et al. Production of acquired immunodeficiency syndrome-associated retrovirus in human and nonhuman cells transfected with an infectious molecular clone. J. Virol. 59, 284-291 (1986).